Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9SN86

- MDHP_ARATH

UniProt

Q9SN86 - MDHP_ARATH

Protein

Malate dehydrogenase, chloroplastic

Gene

At3g47520

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    (S)-malate + NAD+ = oxaloacetate + NADH.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei115 – 1151NADBy similarity
    Binding sitei162 – 1621SubstratePROSITE-ProRule annotation
    Binding sitei168 – 1681SubstratePROSITE-ProRule annotation
    Binding sitei175 – 1751NADBy similarity
    Binding sitei200 – 2001SubstratePROSITE-ProRule annotation
    Binding sitei234 – 2341SubstratePROSITE-ProRule annotation
    Active sitei258 – 2581Proton acceptorBy similarity
    Binding sitei309 – 3091NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi89 – 957NADBy similarity
    Nucleotide bindingi198 – 2003NADBy similarity

    GO - Molecular functioni

    1. L-malate dehydrogenase activity Source: TAIR

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. malate metabolic process Source: InterPro
    3. response to cold Source: TAIR
    4. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciARA:AT3G47520-MONOMER.
    MetaCyc:AT3G47520-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase, chloroplastic (EC:1.1.1.37)
    Alternative name(s):
    pNAD-MDH
    Gene namesi
    Ordered Locus Names:At3g47520
    ORF Names:F1P2.70
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G47520.

    Subcellular locationi

    Plastidchloroplast stroma 2 Publications

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. chloroplast Source: TAIR
    3. chloroplast envelope Source: TAIR
    4. chloroplast stroma Source: TAIR
    5. membrane Source: TAIR
    6. mitochondrion Source: TAIR
    7. plastid Source: TAIR
    8. stromule Source: TAIR
    9. vacuolar membrane Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 8080ChloroplastSequence AnalysisAdd
    BLAST
    Chaini81 – 403323Malate dehydrogenase, chloroplasticPRO_0000224149Add
    BLAST

    Proteomic databases

    PaxDbiQ9SN86.
    PRIDEiQ9SN86.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9SN86.
    GenevestigatoriQ9SN86.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi9226. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SN86.
    SMRiQ9SN86. Positions 83-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 1 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0039.
    HOGENOMiHOG000213792.
    InParanoidiQ9SN86.
    KOiK00026.
    OMAiVEVKGFA.
    PhylomeDBiQ9SN86.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProiIPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR001252. Malate_DH_AS.
    IPR010097. Malate_DH_type1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11540. PTHR11540. 1 hit.
    PfamiPF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
    PROSITEiPS00068. MDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9SN86-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATATSASLF STVSSSYSKA SSIPHSRLQS VKFNSVPSFT GLKSTSLISG    50
    SDSSSLAKTL RGSVTKAQTS DKKPYGFKIN ASYKVAVLGA AGGIGQPLSL 100
    LIKMSPLVST LHLYDIANVK GVAADLSHCN TPSQVRDFTG PSELADCLKD 150
    VNVVVIPAGV PRKPGMTRDD LFNINANIVK TLVEAVAENC PNAFIHIISN 200
    PVNSTVPIAA EVLKKKGVYD PKKLFGVTTL DVVRANTFVS QKKNLKLIDV 250
    DVPVIGGHAG ITILPLLSKT KPSVNFTDEE IQELTVRIQN AGTEVVDAKA 300
    GAGSATLSMA YAAARFVESS LRALDGDGDV YECSFVESTL TDLPFFASRV 350
    KIGKNGLEAV IESDLQGLTE YEQKALEALK VELKASIDKG VAFANKPAAA 400
    AAN 403
    Length:403
    Mass (Da):42,406
    Last modified:May 1, 2000 - v1
    Checksum:i65B54DE66392D229
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 571A → T in CAA74320. (PubMed:9774405)Curated
    Sequence conflicti66 – 661K → N in CAA74320. (PubMed:9774405)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13987 mRNA. Translation: CAA74320.1.
    AL132955 Genomic DNA. Translation: CAB61978.1.
    CP002686 Genomic DNA. Translation: AEE78292.1.
    AY128281 mRNA. Translation: AAM91090.1.
    BT000621 mRNA. Translation: AAN18188.1.
    PIRiT45712.
    T51862.
    RefSeqiNP_190336.1. NM_114620.2.
    UniGeneiAt.20474.

    Genome annotation databases

    EnsemblPlantsiAT3G47520.1; AT3G47520.1; AT3G47520.
    GeneIDi823906.
    KEGGiath:AT3G47520.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13987 mRNA. Translation: CAA74320.1 .
    AL132955 Genomic DNA. Translation: CAB61978.1 .
    CP002686 Genomic DNA. Translation: AEE78292.1 .
    AY128281 mRNA. Translation: AAM91090.1 .
    BT000621 mRNA. Translation: AAN18188.1 .
    PIRi T45712.
    T51862.
    RefSeqi NP_190336.1. NM_114620.2.
    UniGenei At.20474.

    3D structure databases

    ProteinModelPortali Q9SN86.
    SMRi Q9SN86. Positions 83-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 9226. 1 interaction.

    Proteomic databases

    PaxDbi Q9SN86.
    PRIDEi Q9SN86.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G47520.1 ; AT3G47520.1 ; AT3G47520 .
    GeneIDi 823906.
    KEGGi ath:AT3G47520.

    Organism-specific databases

    TAIRi AT3G47520.

    Phylogenomic databases

    eggNOGi COG0039.
    HOGENOMi HOG000213792.
    InParanoidi Q9SN86.
    KOi K00026.
    OMAi VEVKGFA.
    PhylomeDBi Q9SN86.

    Enzyme and pathway databases

    BioCyci ARA:AT3G47520-MONOMER.
    MetaCyc:AT3G47520-MONOMER.

    Miscellaneous databases

    PROi Q9SN86.

    Gene expression databases

    ArrayExpressi Q9SN86.
    Genevestigatori Q9SN86.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProi IPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR001252. Malate_DH_AS.
    IPR010097. Malate_DH_type1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11540. PTHR11540. 1 hit.
    Pfami PF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    TIGRFAMsi TIGR01772. MDH_euk_gproteo. 1 hit.
    PROSITEi PS00068. MDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel, non-redox-regulated NAD-dependent malate dehydrogenase from chloroplasts of Arabidopsis thaliana L."
      Berkemeyer M., Scheibe R., Ocheretina O.
      J. Biol. Chem. 273:27927-27933(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
      Strain: cv. Columbia.
      Tissue: Leaf.
    2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
      Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
      Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: cv. Wassilewskija.

    Entry informationi

    Entry nameiMDHP_ARATH
    AccessioniPrimary (citable) accession number: Q9SN86
    Secondary accession number(s): O81844
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3